Speaker
Description
New recombinant vaccines based on globular protein complexes with fused immunogens have shown amazing efficiency against a number of diseases, e.g., influenza, HIV, HCV, Epstein-Barr, etc. The features of such vaccines: multiple antigen representation, assembly of trimeric viral surface proteins on the surface of 24-meric protein apoferritin at the places of its three-fold channels, and a dual function of a bacterial apoferritin which acts as an adjuvant as well as a carrier. However, in the case of apoferritin-RBD recombinant vaccines the studies showed a necessity of additional adjuvants to achieve an immunological effect in preclinical studies, which might be due to the stochiometric hindrance of RBDs which do not form trimers and might cover apoferritin surface making it hidden from antibodies.
We developed a protocol for obtaining a self-assembling 8-meric apoferritin-RBD recombinant protein complex which has a form-factor of a one third of a sphere, which was confirmed by small-angle X-ray scattering and electron microscopy. The 8-meric apoferritin-RBD might be a potential vaccine in which an internal surface of bacterial apoferritin is available for antibodies due to reduced stochiometric hindrance in comparison with 24-meric apoferritin-RBD vaccines.
We acknowledge the support from the Ministry of Science and Higher Education of the Russian Federation (agreement # 075-03-2023-106, project FSMG-2021-0002).
